JP3377524B2 - 創傷治癒 - Google Patents

創傷治癒

Info

Publication number: JP3377524B2
Authority: JP; Japan
Prior art keywords: tgf; igf; purified; growth factor; bone
Prior art date: 1990-05-30
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Lifetime

Application number

JP51086191A

Other languages

English (en)

Japanese (ja)

Other versions

JPH05507488A (ja

Inventor

ハリーエヌアントニオデス

サミュエルイーリンチ

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Harvard College

Original Assignee

Harvard College

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1990-05-30

Filing date

1991-05-30

Publication date

2003-02-17

1991-05-30 Application filed by Harvard College filed Critical Harvard College

1993-10-28 Publication of JPH05507488A publication Critical patent/JPH05507488A/ja

2003-02-17 Application granted granted Critical

2003-02-17 Publication of JP3377524B2 publication Critical patent/JP3377524B2/ja

2018-02-17 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

Links

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108090001012 Transforming Growth Factor beta Proteins 0.000 claims abstract description 63
102000004887 Transforming Growth Factor beta Human genes 0.000 claims abstract description 62
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Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/30—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
General Health & Medical Sciences (AREA)
Pharmacology & Pharmacy (AREA)
Chemical & Material Sciences (AREA)
Public Health (AREA)
Medicinal Chemistry (AREA)
Engineering & Computer Science (AREA)
Animal Behavior & Ethology (AREA)
Veterinary Medicine (AREA)
Bioinformatics & Cheminformatics (AREA)
Organic Chemistry (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Physical Education & Sports Medicine (AREA)
Immunology (AREA)
Rheumatology (AREA)
Diabetes (AREA)
Molecular Biology (AREA)
Endocrinology (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Orthopedic Medicine & Surgery (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Epidemiology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

JP51086191A 1990-05-30 1991-05-30 創傷治癒 Expired - Lifetime JP3377524B2 (ja)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
US53064990A	1990-05-30	1990-05-30
US530,649		1990-05-30
PCT/US1991/003829 WO1991018622A1 (fr)	1990-05-30	1991-05-30	Cicatrisation

Publications (2)

Publication Number	Publication Date
JPH05507488A JPH05507488A (ja)	1993-10-28
JP3377524B2 true JP3377524B2 (ja)	2003-02-17

Family

ID=24114431

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP51086191A Expired - Lifetime JP3377524B2 (ja)	1990-05-30	1991-05-30	創傷治癒

Country Status (7)

Country	Link
EP (1)	EP0531425B1 (fr)
JP (1)	JP3377524B2 (fr)
AT (1)	ATE222117T1 (fr)
CA (1)	CA2082420C (fr)
DE (1)	DE69133087T2 (fr)
ES (1)	ES2178633T3 (fr)
WO (1)	WO1991018622A1 (fr)

Families Citing this family (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5286643A (en) *	1992-06-24	1994-02-15	The Procter & Gamble Company	Rat osteosarcoma cell line OSR-8
US5286644A (en) *	1992-06-24	1994-02-15	The Procter & Gamble Company	Rat osteosarcoma cell line OSR-2
US5292656A (en) *	1992-06-24	1994-03-08	The Procter & Gamble Company	Rat osteosarcoma cell line OSR-6
US5264358A (en) *	1992-06-24	1993-11-23	The Procter & Gamble Company	Rat osteosarcoma cell line OSR9TR1
US5288628A (en) *	1992-06-24	1994-02-22	The Procter & Gamble Company	Rat osteosarcoma cell line OSR4TR1
US5286645A (en) *	1992-06-24	1994-02-15	The Procter & Gamble Company	Rat osteosarcoma cell line osr3tr1
KR100385293B1 (ko) *	2000-05-13	2003-05-23	주식회사 리젠 바이오텍	βｉｇ-ｈ3의 일부 도메인을 이용한 세포 부착 및 창상치유 방법
GB2369572A (en)	2000-11-29	2002-06-05	Raft Trustees Ltd	Wound treatment composition comprising insulin
JP2014156410A (ja) *	2013-02-14	2014-08-28	Nagoya Univ	組織形成用組成物及びその利用
EP3206670A4 (fr)	2014-10-14	2018-06-20	Samuel Lynch	Compositions pour le traitement de plaies

Family Cites Families (14)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS6034997A (ja) *	1983-05-09	1985-02-22	ジヨージ、ジヨセフ、トダロ	生物学的活性ポリペプチド類
JPS61291521A (ja) *	1983-06-03	1986-12-22	アメリカ合衆国	ヒト血小板もしくはヒト胎盤由来の精製β型トランスホ−ミング成長因子
US4738921A (en) *	1984-09-27	1988-04-19	Eli Lilly And Company	Derivative of the tryptophan operon for expression of fused gene products
ATE84065T1 (de) *	1986-10-09	1993-01-15	Fujisawa Pharmaceutical Co	Expressionsvektor fuer menschlichen insulinaehnlichen wachstumsfaktor-i.
NZ235556A (en) *	1986-11-05	1991-06-25	Ethicon Inc	Breast milk substitute containing recombinant human egf
IE60517B1 (en) *	1986-11-14	1994-07-27	Inst Molecular Biology Inc	Wound healing and bone regeneration
AU1340688A (en) *	1987-01-30	1988-08-24	Techne Corporation	Transforming growth factor-beta
US4885163A (en) *	1987-02-24	1989-12-05	Eli Lilly And Company	Topical use of IGF-II for wound healing
NZ226171A (en) *	1987-09-18	1990-06-26	Ethicon Inc	Gel formulation containing polypeptide growth factor
EP0323842A3 (fr) *	1988-01-07	1990-04-25	Otsuka Pharmaceutical Co., Ltd.	Méthode de purification du facteur de croissance bêta en transformation
US4983581A (en) *	1988-05-20	1991-01-08	Institute Of Molecular Biology, Inc.	Wound healing composition of IGF-I and TGF-β
US4950483A (en) *	1988-06-30	1990-08-21	Collagen Corporation	Collagen wound healing matrices and process for their production
EP0424416B1 (fr) *	1988-07-15	1995-07-19	Central Sydney Area Health Service	Sous-unite labile aux acides d'un complexe proteique de liaison du facteur de croissance analogue a l'insuline
NZ236618A (en) *	1990-01-03	1997-06-24	Ciba Geigy Ag	Treating and preventing osteoporosis using insulin-like growth factor i (igf i) in conjunction with a bone antiresorptive active compound

1991
- 1991-05-30 CA CA002082420A patent/CA2082420C/fr not_active Expired - Lifetime
- 1991-05-30 DE DE69133087T patent/DE69133087T2/de not_active Expired - Lifetime
- 1991-05-30 AT AT91910904T patent/ATE222117T1/de not_active IP Right Cessation
- 1991-05-30 ES ES91910904T patent/ES2178633T3/es not_active Expired - Lifetime
- 1991-05-30 WO PCT/US1991/003829 patent/WO1991018622A1/fr active IP Right Grant
- 1991-05-30 JP JP51086191A patent/JP3377524B2/ja not_active Expired - Lifetime
- 1991-05-30 EP EP91910904A patent/EP0531425B1/fr not_active Expired - Lifetime

Also Published As

Publication number	Publication date
JPH05507488A (ja)	1993-10-28
EP0531425B1 (fr)	2002-08-14
EP0531425A1 (fr)	1993-03-17
ES2178633T3 (es)	2003-01-01
DE69133087T2 (de)	2003-04-03
CA2082420C (fr)	2004-07-20
WO1991018622A1 (fr)	1991-12-12
CA2082420A1 (fr)	1991-12-01
DE69133087D1 (de)	2002-09-19
EP0531425A4 (en)	1997-08-27
ATE222117T1 (de)	2002-08-15

Publication	Publication Date	Title
US4983581A (en)	1991-01-08	Wound healing composition of IGF-I and TGF-β
US5019559A (en)	1991-05-28	Wound healing using PDGF and IGF-II
EP0289584B1 (fr)	1993-05-05	Guerison de plaies et regeneration d'os
US4861757A (en)	1989-08-29	Wound healing and bone regeneration using PDGF and IGF-I
US5035887A (en)	1991-07-30	Wound healing composition of IL-1 and PDGF or IGF-1
CN1027136C (zh)	1994-12-28	伤口的愈合
US5124316A (en)	1992-06-23	Method for periodontal regeneration
EP0382841B1 (fr)	1994-01-26	Cicatrisation de blessures
EP0479799B1 (fr)	1997-08-06	Cicatrisation de plaies
CN1183103A (zh)	1998-05-27	生长因子样活性的肽组合物
JP3377524B2 (ja)	2003-02-17	創傷治癒
US5256644A (en)	1993-10-26	Wound healing using IGF-II and TGF
JPH03502922A (ja)	1991-07-04	インターロイキン‐１蛋白質を含む局所創傷治療用製剤
EP3001810B1 (fr)	2020-03-11	Trap 63

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